Membrane lysis by gramicidin S visualized in red blood cells and giant vesicles

被引：18

作者：

Semrau, S. ^{[1
]}

Monster, M. W. L. ^{[1
]}

van der Knaap, M. ^{[2
]}

Florea, B. I. ^{[2
]}

Schmidt, T. ^{[1
]}

Overhand, M. ^{[2
]}

机构：

[1] Leiden Univ, Huygens Lab, Leiden Inst Phys, Leiden, Netherlands

[2] Leiden Univ, Leiden Inst Chem, Gorlaeus Labs, NL-2300 RA Leiden, Netherlands

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2010年 / 1798卷 / 11期

关键词：

Antimicrobial peptide; Gramicidin S; Hemolysis; Giant vesicle; Membrane material parameter; SUGAR AMINO-ACID; LIPID-MEMBRANES; BILAYER-MEMBRANES; PEPTIDES; MECHANISM; DIFFUSION; SHAPE; ALIGNMENT; MODEL;

D O I：

10.1016/j.bbamem.2010.07.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The cationic amphiphilic antimicrobial peptide gramicidin S (GS) is an effective antibiotic. Its applicability is however restricted to topical infections due to its hemolytic activity. In this study, the process of GS induced hemolysis was investigated in detail for the first time. The morphological changes of red blood cells (RBCs) inflicted by GS were visualized and explained in terms of a physical model. The observed fast rupture events were further investigated with giant unilamellar vesicles (GUVs) as model systems for RBCs. Measurements of membrane fluctuations in GUVs revealed that the membrane surface tension was increased after incubation with GS. These findings are in agreement with the hypothesis that amphiphilic peptides induce membrane rupture by an increase in membrane tension. (C) 2010 Elsevier B.V. All rights reserved.

引用

页码：2033 / 2039

页数：7

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